ID A0A3D9UB58_9GAMM Unreviewed; 384 AA.
AC A0A3D9UB58;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 18-JUN-2025, entry version 25.
DE SubName: Full=Dihydroorotase {ECO:0000313|EMBL:REF26629.1};
GN ORFNames=BDD26_1299 {ECO:0000313|EMBL:REF26629.1};
OS Xenorhabdus cabanillasii.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Enterobacterales; Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351673 {ECO:0000313|EMBL:REF26629.1, ECO:0000313|Proteomes:UP000256294};
RN [1] {ECO:0000313|EMBL:REF26629.1, ECO:0000313|Proteomes:UP000256294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17905 {ECO:0000313|EMBL:REF26629.1,
RC ECO:0000313|Proteomes:UP000256294};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:REF26629.1}.
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DR EMBL; QTUB01000001; REF26629.1; -; Genomic_DNA.
DR RefSeq; WP_115825875.1; NZ_QTUB01000001.1.
DR AlphaFoldDB; A0A3D9UB58; -.
DR Proteomes; UP000256294; Unassembled WGS sequence.
DR GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 1.
DR InterPro; IPR020043; Deacetylase_Atu3266-like.
DR InterPro; IPR047601; EF_0837-like.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR NCBIfam; TIGR03583; EF_0837; 1.
DR NCBIfam; NF006689; PRK09237.1; 1.
DR PANTHER; PTHR42717; DIHYDROOROTASE-RELATED; 1.
DR PANTHER; PTHR42717:SF1; IMIDAZOLONEPROPIONASE AND RELATED AMIDOHYDROLASES; 1.
DR Pfam; PF22647; EF_0837-like_N; 1.
DR PIRSF; PIRSF039004; ADE_EF_0837; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR039004-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000256294};
KW Zinc {ECO:0000256|PIRSR:PIRSR039004-1}.
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 153
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 209
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-1"
FT SITE 155
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-3"
FT MOD_RES 153
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR039004-2"
SQ SEQUENCE 384 AA; 41968 MW; B2382E53562395E5 CRC64;
MYDLIIRQGK LINGDITDII VNDGRVIDIG PAVATGLNAS KEIDLCGHYH ISAGWIDAHT
HCYPKSPLYF DDPDLIGVTK GVTTVVDAGS AGADDIDPFY HAARKAKTHV YAFLNIARTG
IRNQNELADL TQIDDNSLQD AVKRHAGFVI GLKARMSKSV VGENGLQPLL KAKMMQQKNG
LPLMVHIGNP PPNLEEIADQ LTKGDIITHC FNSKPNRILD NEGHLKAAIQ RAIERGVILD
VGHGTESFSF RIAEQAIRSA AYPHMISSDI YQRNRIDGPV YSLATVMNKF LSMGVSPEQV
LNSVTINAAN FLRLSRKGRL EHGFDGDITI FELKNQHIEL VDAEGEVRVG TQQFIPIAAI
ISGTDIVVAD PIVTDRSTHN DISV
//
